ID   SYL_CHESB               Reviewed;         871 AA.
AC   Q11DE4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=Meso_3209;
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNC1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC         tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC         COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR   EMBL; CP000390; ABG64581.1; -; Genomic_DNA.
DR   RefSeq; WP_011582522.1; NC_008254.1.
DR   AlphaFoldDB; Q11DE4; -.
DR   SMR; Q11DE4; -.
DR   STRING; 266779.Meso_3209; -.
DR   EnsemblBacteria; ABG64581; ABG64581; Meso_3209.
DR   KEGG; mes:Meso_3209; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   PANTHER; PTHR43740; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..871
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009369"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           629..633
FT                   /note="'KMSKS' region"
FT   BINDING         632
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   871 AA;  97963 MW;  BCC50C7EB253FA83 CRC64;
     MATERYNPRT SEPRWQKAWE EARLFETKND DGRPTYYVLE MFPYPSGRIH IGHTRNYTMG
     DVVARYKRAK GYNVLHPMGW DAFGMPAENA AIQNKIHPKE WTYDNIATMR SQLKMMGLSL
     DWAREFATCD VDYYHRQQML FIDFYKKGLV RRKTSKVNWD PVEQTVLANE QVIDGRGWRS
     GALVEQRELA QWFFKITDYA EDLLSAIDGL DDWPEKVRLM QRNWIGRSEG LSIRWALAED
     TAPAGVGELE VYTTRPDTIF GASFLAVAPD HPLARKAAEG NPALATFIEE CRHMGTSVAA
     LETAEKKGFD TGIRVKHPFD AEWTLPVYVA NFVLMEYGTG AIFGCPSGDQ RDFDFANKYG
     LPVIPVVMPE GADAATFEIT AEPYVDDGVM LNSRFLDGMS NKEAFEEVAS RLEKETLDGK
     PVAKRKVNFR LRDWGVSRQR YWGCPIPMIH CDTCGVVPVP KEELPVKLPD DVDFDRPGNP
     LDRHPTWRHV KCPQCGADAR RETDTMDTFV DSSWYFARFT SPHADSPVEK DVVNRWLPVD
     QYIGGIEHAI LHLLYSRFFT RAMRDTGHLD LAEPFKGLFT QGMVVHETYR AEDGRWLTPA
     EVRIEGSAGE RRAFEIATGK EVAIGPLEKM SKSKKNTVSP EDITESFGAD TARWFMLSDS
     PPERDVEWTD DGAAGAHRFV QRAWRLITEA APAIGDITPK AARDGDAAAI SKPAHKALKA
     VGEDIERLAF NRAIARIHEL VNDLQGPFAG LDKADEETRA AAREATEILI HLIAPFMPHL
     AEECWAAIGG KDLVAASRWP DFDPELVLDN LIVLPVQING KKRGDLTIAR EADQAAVEKA
     VLELDFVQKA LNGAPPRKVI VVSQRIVNVV A